Discovery May Revolutionize Therapy In Muscular Dystrophy And Other Skeletal Mus

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Discovery May Revolutionize Therapy In Muscular Dystrophy And Other Skeletal

Muscle Disorders

http://www.medicalnewstoday.com/articles/153499.php

Researchers at UMDNJ- Wood Medical School are a step closer to

treating, and perhaps preventing, muscle damage caused by disease and aging. In

their study, published in the June issue of Journal of Biological Chemistry, the

scientists have linked the newly discovered protein MG53 to a pathway that

repairs human muscle tissue along with the proteins caveolin-3 (Cav3) and

dysferlin. Prior to this study, the underlying interactions that inhibited

membrane repair in muscle tissue were unknown. Linking these proteins creates a

mechanism that allows damaged membranes to be repaired, which may transform

treatment for patients who suffer from severe complications of diseases such as

muscular dystrophy, as well as cardiovascular disorders and conditions related

to advancing age.

The study was led by Jianjie Ma, PhD, professor of physiology and biophysics at

UMDNJ- Wood Medical School, in collaboration with Professor

Hiroshi Takeshima at Kyoto University, Japan.

According to Dr. Ma, human cells are continuously injured and naturally repaired

through the life span. For instance, micro tears can occur as muscles contract

within the body during normal everyday activities. However, diseases such as

diabetes, cardiovascular disorders and muscular dystrophy, and even aging,

compromise the method in which the body repairs its own tissues, resulting in

severe damage. His research team announced in December 2008 that it had

discovered MG53 as a key initiator of membrane repair in damaged tissue, making

it the first group to specifically pinpoint a protein responsible for promoting

cell repair.

In the new study, the team's research has revealed that MG53 acts first as the

initial sensor of damaged tissue during the repair process. Then, through its

interaction with Cav3, MG53 recruits intracellular vesicles to the injury site

in the membrane, acting as a trafficking agent in the repair process. The

vesicles interact with dysferlin to fuse with the membrane, thereby creating a

repair patch and allowing for normal membrane function.

" Dysferlin has previously been linked to muscle repair, but our findings show

that it can not complete the process when MG53 is absent, " said Dr. Ma. " The

discovery of MG53 as a necessary element in the repair mechanism provides a

foundation in which to study the broader implications of how MG53 fits into the

next generation of therapeutic treatments for patients with muscle and

cardiovascular disease. We are also looking at its potential to prevent damage

from ever occurring. "

In advance of its publication in the June issue of the Journal of Biological

Chemistry, in which it was designated a paper of the week, the investigation

appeared online in May as a featured research study. The research was supported

by grants from the National Institutes of Health, the Ministry of Education,

Science, Sports and Culture of Japan and the American Heart Association.